1,25(OH)2D3 regulates collagen quality in an osteoblastic cell culture system.
The active form of vitamin D, 1,25(OH)(2)D(3), has a broad range of effects on bone, however, its role in the quality of bone matrix is not well understood. In this study, using an osteoblastic cell (MC3T3-E1) culture system, the effects of 1,25(OH)(2)D(3) on collagen cross-linking and related enzymes, i.e., lysyl hydroxylases (LH1-3) and lysyl oxidases (LOX, LOXL1-4), were examined and compared to controls where cells were treated with cholecalciferol or ethanol. When compared to the controls, gene expressions of LH1, LH2b and LOXL2 were significantly upregulated by 1,25(OH)(2)D(3) up to 72h of culture. In addition, hydroxylysine (Hyl), Hyl aldehyde (Hyl(ald)), Hyl(ald)-derived cross-links and a total number of cross-links of collagen were significantly higher and the cross-link maturation was accelerated in the 1,25(OH)(2)D(3) treated group. These results demonstrate that 1,25(OH)(2)D(3) directly regulates collagen cross-linking in this culture system likely by upregulating gene expression of specific LH and LOX enzymes.
Nagaoka
Hideaki
H
CB#7455, Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, USA; Department of Maxillofacial Surgery, Nihon University School of Dentistry at Matsudo, Chiba 271-8587, Japan.
Mochida
Yoshiyuki
Y
CB#7455, Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, USA.
Atsawasuwan
Phimon
P
CB#7455, Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, USA.
Kaku
Masaru
M
CB#7455, Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, USA.
Kondoh
Toshirou
T
Department of Maxillofacial Surgery, Nihon University School of Dentistry at Matsudo, Chiba 271-8587, Japan.
Yamauchi
Mitsuo
M
CB#7455, Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, USA. Electronic address: Mitsuo_Yamauchi@dentistry.unc.edu.
D017398:Alternative Splicing; D000818:Animals; D015415:Biomarkers; D002117:Calcitriol / Q000494:pharmacology / Q000502:physiology*; D002460:Cell Line; D002762:Cholecalciferol / Q000494:pharmacology; D003094:Collagen / Q000378:metabolism*; D000431:Ethanol / Q000494:pharmacology; D015870:Gene Expression / Q000187:drug effects; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D051379:Mice; D010006:Osteoblasts / Q000187:drug effects / Q000378:metabolism*; D010012:Osteogenesis; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D008249:Protein-Lysine 6-Oxidase / Q000235:genetics / Q000378:metabolism
D015415:Biomarkers; D007527:Isoenzymes; D002762:Cholecalciferol; D000431:Ethanol; D003094:Collagen; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase; D008249:Protein-Lysine 6-Oxidase; D002117:Calcitriol; D008239:Lysine